RS12_TROWT
ID RS12_TROWT Reviewed; 124 AA.
AC Q83FN9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=TWT_677;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
CC -!- FUNCTION: With S4 and S5 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}.
CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are
CC involved in tRNA selection in the A site and with the mRNA backbone.
CC Located at the interface of the 30S and 50S subunits, it traverses the
CC body of the 30S subunit contacting proteins on the other side and
CC probably holding the rRNA structure together. The combined cluster of
CC proteins S8, S12 and S17 appears to hold together the shoulder and
CC platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_00403}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC S17. May interact with IF1 in the 30S initiation complex.
CC {ECO:0000255|HAMAP-Rule:MF_00403}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00403}.
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DR EMBL; AE014184; AAO44774.1; -; Genomic_DNA.
DR RefSeq; WP_011096633.1; NC_004572.3.
DR AlphaFoldDB; Q83FN9; -.
DR SMR; Q83FN9; -.
DR STRING; 203267.TWT_677; -.
DR EnsemblBacteria; AAO44774; AAO44774; TWT_677.
DR GeneID; 67388472; -.
DR KEGG; twh:TWT_677; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_11; -.
DR OMA; SPALEKC; -.
DR OrthoDB; 1707228at2; -.
DR Proteomes; UP000002200; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd03368; Ribosomal_S12; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_S12/S23.
DR InterPro; IPR005679; Ribosomal_S12_bac.
DR PANTHER; PTHR11652; PTHR11652; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR PRINTS; PR01034; RIBOSOMALS12.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00981; rpsL_bact; 1.
DR PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146348"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
SQ SEQUENCE 124 AA; 13840 MW; BC0A500D1F9408F0 CRC64;
MPTIQQLVRK GRRPKVNKTK SPALRGNPQQ RGVCSRVYTT TPKKPNSALR KVARVKLSNG
TEVTVYIPGE GHNLQEHSIV LVRGGRVKDL PGVRYKVVRG ALDAQAVKDR KQARSRYGAK
MEKK
